ID   PRPE_SALTY              Reviewed;         628 AA.
AC   P55912;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   11-JUL-2001, sequence version 2.
DT   03-AUG-2022, entry version 106.
DE   RecName: Full=Propionate--CoA ligase;
DE            EC=6.2.1.17;
DE   AltName: Full=Propionyl-CoA synthetase;
GN   Name=prpE; OrderedLocusNames=STM0371;
OS   Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=99287;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=LT2;
RX   PubMed=9006051; DOI=10.1128/jb.179.3.928-940.1997;
RA   Horswill A.R., Escalante-Semerena J.C.;
RT   "Propionate catabolism in Salmonella typhimurium LT2: two divergently
RT   transcribed units comprise the prp locus at 8.5 centisomes, prpR encodes a
RT   member of the sigma-54 family of activators, and the prpBCDE genes
RT   constitute an operon.";
RL   J. Bacteriol. 179:928-940(1997).
RN   [2]
RP   SEQUENCE REVISION TO 464 AND C-TERMINUS, AND FUNCTION.
RC   STRAIN=LT2;
RX   PubMed=10411265; DOI=10.1099/13500872-145-6-1381;
RA   Horswill A.R., Escalante-Semerena J.C.;
RT   "The prpE gene of Salmonella typhimurium LT2 encodes propionyl-CoA
RT   synthetase.";
RL   Microbiology 145:1381-1388(1999).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX   PubMed=11677609; DOI=10.1038/35101614;
RA   McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA   Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA   Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA   Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA   Wilson R.K.;
RT   "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL   Nature 413:852-856(2001).
RN   [4]
RP   FUNCTION, AND PATHWAY.
RX   PubMed=10482501; DOI=10.1128/jb.181.18.5615-5623.1999;
RA   Horswill A.R., Escalante-Semerena J.C.;
RT   "Salmonella typhimurium LT2 catabolizes propionate via the 2-methylcitric
RT   acid cycle.";
RL   J. Bacteriol. 181:5615-5623(1999).
CC   -!- FUNCTION: Catalyzes the synthesis of propionyl-CoA from propionate and
CC       CoA. Also converts acetate to acetyl-CoA but with a lower specific
CC       activity. {ECO:0000269|PubMed:10411265, ECO:0000269|PubMed:10482501}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + CoA + propanoate = AMP + diphosphate + propanoyl-CoA;
CC         Xref=Rhea:RHEA:20373, ChEBI:CHEBI:17272, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:57392,
CC         ChEBI:CHEBI:456215; EC=6.2.1.17;
CC   -!- PATHWAY: Organic acid metabolism; propanoate degradation.
CC       {ECO:0000269|PubMed:10482501}.
CC   -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC       {ECO:0000305}.
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DR   EMBL; U51879; AAC44817.2; -; Genomic_DNA.
DR   EMBL; AE006468; AAL19325.1; -; Genomic_DNA.
DR   RefSeq; NP_459366.1; NC_003197.2.
DR   RefSeq; WP_000010229.1; NC_003197.2.
DR   AlphaFoldDB; P55912; -.
DR   SMR; P55912; -.
DR   STRING; 99287.STM0371; -.
DR   PaxDb; P55912; -.
DR   EnsemblBacteria; AAL19325; AAL19325; STM0371.
DR   GeneID; 1251890; -.
DR   KEGG; stm:STM0371; -.
DR   PATRIC; fig|99287.12.peg.393; -.
DR   HOGENOM; CLU_000022_3_5_6; -.
DR   OMA; YSSLDWA; -.
DR   PhylomeDB; P55912; -.
DR   BioCyc; MetaCyc:MON-62; -.
DR   BioCyc; SENT99287:STM0371-MON; -.
DR   UniPathway; UPA00946; -.
DR   Proteomes; UP000001014; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0050218; F:propionate-CoA ligase activity; IDA:CACAO.
DR   GO; GO:0019629; P:propionate catabolic process, 2-methylcitrate cycle; IEA:InterPro.
DR   Gene3D; 3.30.300.30; -; 1.
DR   Gene3D; 3.40.50.12780; -; 1.
DR   InterPro; IPR032387; ACAS_N.
DR   InterPro; IPR025110; AMP-bd_C.
DR   InterPro; IPR045851; AMP-bd_C_sf.
DR   InterPro; IPR020845; AMP-binding_CS.
DR   InterPro; IPR000873; AMP-dep_Synth/Lig.
DR   InterPro; IPR042099; ANL_N_sf.
DR   InterPro; IPR012694; Propion_PrpE.
DR   Pfam; PF16177; ACAS_N; 1.
DR   Pfam; PF00501; AMP-binding; 1.
DR   Pfam; PF13193; AMP-binding_C; 1.
DR   TIGRFAMs; TIGR02316; propion_prpE; 1.
DR   PROSITE; PS00455; AMP_BINDING; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Ligase; Nucleotide-binding; Reference proteome.
FT   CHAIN           1..628
FT                   /note="Propionate--CoA ligase"
FT                   /id="PRO_0000193189"
SQ   SEQUENCE   628 AA;  69334 MW;  0C30F0C783731D9E CRC64;
     MSFSEFYQRS INEPEAFWAE QARRIDWRQP FTQTLDHSRP PFARWFCGGT TNLCHNAVDR
     WRDKQPEALA LIAVSSETDE ERTFTFSQLH DEVNIVAAML LSLGVQRGDR VLVYMPMIAE
     AQITLLACAR IGAIHSVVFG GFASHSVAAR IDDARPALIV SADAGARGGK ILPYKKLLDD
     AIAQAQHQPK HVLLVDRGLA KMAWVDGRDL DFATLRQQHL GASVPVAWLE SNETSCILYT
     SGTTGKPKGV QRDVGGYAVA LATSMDTIFG GKAGGVFFCA SDIGWVVGHS YIVYAPLLAG
     MATIVYEGLP TYPDCGVWWK IVEKYQVNRM FSAPTAIRVL KKFPTAQIRN HDLSSLEALY
     LAGEPLDEPT ASWVTETLGV PVIDNYWQTE SGWPIMALAR ALDDRPSRLG SPGVPMYGYN
     VQLLNEVTGE PCGINEKGML VIEGPLPPGC IQTIWGDDAR FVKTYWSLFN RQVYATFDWG
     IRDAEGYYFI LGRTDDVINI AGHRLGTREI EESISSYPNV AEVAVVGIKD ALKGQVAVAF
     VIPKQSDTLA DREAARDEEN AIMALVDNQI GHFGRPAHVW FVSQLPKTRS GKMLRRTIQA
     ICEGRDPGDL TTIDDPASLQ QIRQAIEE